ATP6_PICAN
ID ATP6_PICAN Reviewed; 259 AA.
AC C0HK57;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=ATP synthase subunit a {ECO:0000250|UniProtKB:P00854};
DE AltName: Full=F-ATPase protein 6 {ECO:0000250|UniProtKB:P00854};
DE Flags: Precursor;
GN Name=ATP6 {ECO:0000250|UniProtKB:P00854};
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730 {ECO:0000303|PubMed:25759169};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 8-25, IDENTIFICATION
RP IN ATP SYNTHASE COMPLEX, FUNCTION OF ATPASE COMPLEX, SUBUNIT, SUBCELLULAR
RP LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=A16 / NCYC 2310 {ECO:0000303|PubMed:25759169};
RX PubMed=25759169; DOI=10.1042/bj20150197;
RA Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA Fearnley I.M., Walker J.E.;
RT "The purification and characterization of ATP synthase complexes from the
RT mitochondria of four fungal species.";
RL Biochem. J. 468:167-175(2015).
RN [2] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=A16 / NCYC 2310 {ECO:0000303|Ref.2};
RA Fearnley I.M.;
RL Submitted (AUG-2016) to UniProtKB.
RN [3] {ECO:0007744|PDB:5LQX, ECO:0007744|PDB:5LQY, ECO:0007744|PDB:5LQZ}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS) OF MONOMERIC ATP SYNTHASE
RP COMPLEX IN COMPLEX WITH BOVINE ATPIF1, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27791192; DOI=10.1073/pnas.1615902113;
RA Vinothkumar K.R., Montgomery M.G., Liu S., Walker J.E.;
RT "Structure of the mitochondrial ATP synthase from Pichia angusta determined
RT by electron cryo-microscopy.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:12709-12714(2016).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain (PubMed:25759169). F-type ATP synthases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the membrane
CC proton channel, linked together by a central stalk and a peripheral
CC stalk (PubMed:27791192). During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation (By similarity). Key
CC component of the proton channel; it may play a direct role in the
CC translocation of protons across the membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q36258, ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27791192}.
CC -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC F(1) and the membrane-embedded component F(0), linked together by a
CC central stalk and a peripheral stalk (PubMed:27791192). The central
CC stalk, also called rotor shaft, is often seen as part of F(1)
CC (PubMed:27791192). The peripheral stalk is seen as part of F(0). F(0)
CC contains the membrane channel next to the rotor (PubMed:27791192). F-
CC type ATP synthases form dimers but each monomer functions independently
CC in ATP generation (By similarity). The dimer consists of 18 different
CC polypeptides: ATP1 (subunit alpha, part of F(1), 3 molecules per
CC monomer), ATP2 (subunit beta, part of F(1), 3 molecules per monomer),
CC ATP3 (subunit gamma, part of the central stalk), ATP4 (subunit b, part
CC of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP, part of the
CC peripheral stalk), ATP6 (subunit a, part of the peripheral stalk), ATP7
CC (subunit d, part of the peripheral stalk), ATP8 (subunit 8, part of the
CC peripheral stalk), OLI1 (subunit c, part of the rotor, 10 molecules per
CC monomer), ATP14 (subunit h, part of the peripheral stalk), ATP15
CC (subunit epsilon, part of the central stalk), ATP16 (subunit delta,
CC part of the central stalk), ATP17 (subunit f, part of the peripheral
CC stalk), ATP18 (subunit i/j, part of the peripheral stalk)
CC (PubMed:27791192, PubMed:25759169). Dimer-specific subunits are ATP19
CC (subunit k, at interface between monomers), ATP20 (subunit g, at
CC interface between monomers), TIM11 (subunit e, at interface between
CC monomers) (By similarity). Also contains subunit L (PubMed:25759169).
CC {ECO:0000250|UniProtKB:Q36258, ECO:0000269|PubMed:25759169,
CC ECO:0000269|PubMed:27791192}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:27791192}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:27791192}. Note=The F-type ATP synthase complex is
CC anchored in the mitochondrial inner membrane via the F(0) domain with
CC the F(1) domain and the peripheral stalk extending into the
CC mitochondrial matrix. {ECO:0000305|PubMed:27791192}.
CC -!- MASS SPECTROMETRY: Mass=27570; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:25759169};
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR PDB; 5LQX; EM; 7.90 A; Y=8-259.
DR PDB; 5LQY; EM; 7.80 A; Y=8-259.
DR PDB; 5LQZ; EM; 7.00 A; Y=8-259.
DR PDBsum; 5LQX; -.
DR PDBsum; 5LQY; -.
DR PDBsum; 5LQZ; -.
DR AlphaFoldDB; C0HK57; -.
DR SMR; C0HK57; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..7
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:25759169"
FT /id="PRO_0000445331"
FT CHAIN 8..259
FT /note="ATP synthase subunit a"
FT /evidence="ECO:0000269|PubMed:25759169, ECO:0000269|Ref.2"
FT /id="PRO_0000445332"
FT TRANSMEM 36..56
FT /note="Helical; Name=aH1"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=aH3"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=aH4"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..206
FT /note="Helical; Name=aH5"
FT /evidence="ECO:0000305|PubMed:27791192"
FT TRANSMEM 211..253
FT /note="Helical; Name=aH6"
FT /evidence="ECO:0000305|PubMed:27791192"
SQ SEQUENCE 259 AA; 28401 MW; 5642BFDD4FEF143D CRC64;
MTNNYINSPL DQFIINNLLE INSPFLNLST LNFSTFSLYT LFVVLVISLT FILSIGGESN
NLVKGSNWLI AIEAIFDTIL NMVKGQIGGS VYGRYVPLVY TLFTFILVAN LIGMVPYNFA
LSASLIYIIG ISVSLWIGLT ILGLFLNKAV FFSLFVPSGT PLPLVPVLVL IELLSYTARA
ISLGLRLAAN TLSGHLLMSI LGNLVKNLMS INYFTFIFGL IPLAGIFAIV ILEFAIACIQ
AYVFAILTSS YLKDSIYLH
